Hydrolysis amino acids

GC requires low molecular weight molecules, and the macromolecular nature of proteinaceous materials (made up of 21 amino acids covalently condensed) means that they are typically too large to be readily identifiable and time consuming pretreatments of the sample are required. In order to free the amino acids, hydrolysis is required. Subsequent steps of purification to eliminate pigment interferences are also often necessary. Consequently sample pretreatments must be carefully carried out to reduce the risk of loss and/or contamination of the sample. 

In addition to the above-mentioned reactions, metal complexes catalyze decarboxylation of keto acids, hydrolysis of esters of amino acids, hydrolysis of peptides, hydrolysis of Schiff bases, formation of porphyrins, oxidation of thiols, and so on. However, polymer-metal complexes have not yet been applied to these reactions. 

Tryptic Maps of Relaxin and Relaxin B-chain. Digestion of the A-chain of human relaxin with trypsin can theoretically result in the release of five fragments that of the B-chain in the release of six fragments as illustrated in Table II. A typical tryptic map of relaxin B-chain is shown in Figure 2. The peptide was reduced and carboxymethylated with iodoacetic acid before enzymatic digestion. The peptide assignments were made after analysis of the peaks by amino acid hydrolysis for amino acid composition and confirmed by fast atom bombardment mass spectrometry (FAB-MS) as shown in Table IH... 

Additional evidence for a bacterial contribution to HMW DOM proteins comes from molecular-level analyses of dissolved amino acids. Hydrolysis of HMW DON releases 11-29% of the nitrogen as amino acids (McCarthy et al., 1996). Specific amino acids include common protein amino acids, as well as /3-alanine and y-aminobutyric acid which are nonprotein amino acid degradation products. The distribution of amino acids is similar to that of fresh plankton cells, suspended particulate matter, and total dissolved amino acids. However, stereochemical analyses show HMW DOM amino acids to be elevated in the D-enantiomer, with d/l ratios for alanine, aspartic acid, glutamic acids, and serine ranging from 0.1 to 0.5 (McCarthy et al., 1998). Racemization of phytoplankton-derived L-amino acids is too slow at ocean temperatures to yield such high D/L ratios, but bacteria can synthesize D-amino acids, and it is likely that the D-amino acids in HMW DOM result from bacterial bioploymers rich in these particular amino acids. The high dA ratios of some amino acids and the abundance of amide nitrogen in HMW DOM N-NMR spectra led McCarthy et al. (1998) to... 

Short-time proteolysis amino acids Hydrolysis into large Formation of peptide of 30 0 0... 

The authors are pleased to acknowledge the analytical assistance of Robert Rinehart of Huffman Laboratories, of Wheatridge, Colorado. Jim Beaudry engineered all the RF. generator and activator circuitry, and for whose assistance we are deeply indebted. Cyril Ponnamperuma of NASA, Ames Research Center, kindly provided the amino acid hydrolysis results on our material. Finally, technical discussions with Richard Bersin were most helpful. 

An internal standard needs to be added as early as possible in the procedure so that the maximum number of steps can be monitored. For amino acid hydrolysis, this should be right after the sample is quantitatively aliquoted and definitely before hydrolysis or oxidation. 

D. Enzymes Involved In Af-Carbamoyl Amino Acid Hydrolysis... 

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